PMID:9303320
| Citation |
Schmitt, E, Mechulam, Y, Fromant, M, Plateau, P and Blanquet, S (1997) Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase. EMBO J. 16:4760-9 |
|---|---|
| Abstract |
Peptidyl-tRNA hydrolase activity from Escherichia coli ensures the recycling of peptidyl-tRNAs produced through abortion of translation. This activity, which is essential for cell viability, is carried out by a monomeric protein of 193 residues. The structure of crystalline peptidyl-tRNA hydrolase could be solved at 1.2 A resolution. It indicates a single alpha/beta globular domain built around a twisted mixed beta-sheet, similar to the central core of an aminopeptidase from Aeromonas proteolytica. This similarity allowed the characterization by site-directed mutagenesis of several residues of the active site of peptidyl-tRNA hydrolase. These residues, strictly conserved among the known peptidyl-tRNA hydrolase sequences, delineate a channel which, in the crystal, is occupied by the C-end of a neighbouring peptidyl-tRNA hydrolase molecule. Hence, several main chain atoms of three residues belonging to one peptidyl-tRNA hydrolase polypeptide establish contacts inside the active site of another peptidyl-tRNA hydrolase molecule. Such an interaction is assumed to represent the formation of a complex between the enzyme and one product of the catalysed reaction. |
| Links |
PubMed PMC1170102 Online version:10.1093/emboj/16.15.4760 |
| Keywords |
Aeromonas/enzymology; Amino Acid Sequence; Binding Sites/genetics; Carboxylic Ester Hydrolases/chemistry; Carboxylic Ester Hydrolases/genetics; Carboxylic Ester Hydrolases/metabolism; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Protein Structure, Secondary; Sequence Homology, Amino Acid; Species Specificity; Substrate Specificity |
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